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Volumn 268, Issue 1, 2007, Pages 52-58

Dimeric structure of nucleoside diphosphate kinase from moderately halophilic bacterium: Contrast to the tetrameric Pseudomonas counterpart

Author keywords

Dimer; Halomonas; Halophilic; Nucleoside diphosphate kinase; Pseudomonas; Subunit

Indexed keywords

DIMER; NUCLEOSIDE DIPHOSPHATE KINASE; SODIUM CHLORIDE; TETRAMER;

EID: 33846652454     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2007.00626.x     Document Type: Article
Times cited : (20)

References (22)
  • 1
    • 0042476350 scopus 로고    scopus 로고
    • Accuracy in multiangle light scattering measurements for molar mass and radius estimations. Model calculations and experiments
    • Andersson M, Wittgren B & Wahlund KG (2003) Accuracy in multiangle light scattering measurements for molar mass and radius estimations. Model calculations and experiments. Anal Chem 75: 4279-4291.
    • (2003) Anal Chem , vol.75 , pp. 4279-4291
    • Andersson, M.1    Wittgren, B.2    Wahlund, K.G.3
  • 3
    • 0035970769 scopus 로고    scopus 로고
    • NaCl-activated nucleoside diphosphate kinase from extremely halophilic archaeon, Halobacterium salinarum, maintains native conformation without salt
    • Ishibashi M, Tokunaga H, Hiratsuka K, Yonezawa Y, Tsurumaru H, Arakawa T & Tokunaga M (2001) NaCl-activated nucleoside diphosphate kinase from extremely halophilic archaeon, Halobacterium salinarum, maintains native conformation without salt. FEBS Lett 493: 134-138.
    • (2001) FEBS Lett , vol.493 , pp. 134-138
    • Ishibashi, M.1    Tokunaga, H.2    Hiratsuka, K.3    Yonezawa, Y.4    Tsurumaru, H.5    Arakawa, T.6    Tokunaga, M.7
  • 4
    • 0037027525 scopus 로고    scopus 로고
    • Secondary and quaternary structural transition of the halophilic archaeon nucleoside diphosphate kinase under high- and low-salt conditions
    • Ishibashi M, Arakawa T, Philo JS, Sakashita K, Yonezawa Y, Tokunaga H & Tokunaga M (2002) Secondary and quaternary structural transition of the halophilic archaeon nucleoside diphosphate kinase under high- and low-salt conditions. FEMS Microbiol Lett 216: 235-241.
    • (2002) FEMS Microbiol Lett , vol.216 , pp. 235-241
    • Ishibashi, M.1    Arakawa, T.2    Philo, J.S.3    Sakashita, K.4    Yonezawa, Y.5    Tokunaga, H.6    Tokunaga, M.7
  • 5
    • 3142568419 scopus 로고    scopus 로고
    • Facilitated folding and subunit assembly in Escherichia coli and in vitro of nucleoside diphosphate kinase from extremely halophilic archaeon conferred by amino-terminal extension containing hexa-His-tag
    • Ishibashi M, Arakawa T & Tokunaga M (2004) Facilitated folding and subunit assembly in Escherichia coli and in vitro of nucleoside diphosphate kinase from extremely halophilic archaeon conferred by amino-terminal extension containing hexa-His-tag. FEBS Lett 570: 87-92.
    • (2004) FEBS Lett , vol.570 , pp. 87-92
    • Ishibashi, M.1    Arakawa, T.2    Tokunaga, M.3
  • 6
    • 24944585182 scopus 로고    scopus 로고
    • Characterization of arginine as a solvent additive: A halophilic enzyme as a model protein
    • Ishibashi M, Tsumoto K, Ejima D, Arakawa T & Tokunaga M (2005) Characterization of arginine as a solvent additive: a halophilic enzyme as a model protein. Protein Pept Lett 12: 649-653.
    • (2005) Protein Pept Lett , vol.12 , pp. 649-653
    • Ishibashi, M.1    Tsumoto, K.2    Ejima, D.3    Arakawa, T.4    Tokunaga, M.5
  • 8
    • 0038546599 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinases: Genes and protein functions
    • Kimura N (2003) Nucleoside diphosphate kinases: genes and protein functions. J Bioenerg Biomembr 35: 3-4.
    • (2003) J Bioenerg Biomembr , vol.35 , pp. 3-4
    • Kimura, N.1
  • 9
    • 0016139829 scopus 로고
    • Salt-dependent properties of proteins from extremely halophilic bacteia
    • Lanyi JK (1974) Salt-dependent properties of proteins from extremely halophilic bacteia. Bacteriol Rev 38: 272-290.
    • (1974) Bacteriol Rev , vol.38 , pp. 272-290
    • Lanyi, J.K.1
  • 10
    • 0033805046 scopus 로고    scopus 로고
    • The nucleoside diphosphate kinases 1973-2000
    • Lascu I (2000) The nucleoside diphosphate kinases 1973-2000. J Bioenerg Biomembr 32: 213-214.
    • (2000) J Bioenerg Biomembr , vol.32 , pp. 213-214
    • Lascu, I.1
  • 12
  • 13
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: Proteins with a grain of salt
    • Mevarech M, Frolow F & Gloss LM (2000) Halophilic enzymes: proteins with a grain of salt. Biophys Chem 86: 155-164.
    • (2000) Biophys Chem , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 15
    • 0014026949 scopus 로고
    • Erythrocytic nucleoside diphosphokinase. II. Isolation and kinetics
    • Mourad N & Parks RE Jr (1966) Erythrocytic nucleoside diphosphokinase. II. Isolation and kinetics. J Biol Chem 241: 271-278.
    • (1966) J Biol Chem , vol.241 , pp. 271-278
    • Mourad, N.1    Parks Jr, R.E.2
  • 16
    • 23944462637 scopus 로고    scopus 로고
    • How to be moderately halophilic with broad salt tolerance: Clues from the genome of chromohalobacter salexigens
    • Oren A, Larimer F, Richardson P, Lapidus A & Csonka LN (2005) How to be moderately halophilic with broad salt tolerance: clues from the genome of chromohalobacter salexigens. Extremophiles 9: 275-279.
    • (2005) Extremophiles , vol.9 , pp. 275-279
    • Oren, A.1    Larimer, F.2    Richardson, P.3    Lapidus, A.4    Csonka, L.N.5
  • 17
    • 0015218591 scopus 로고
    • Purification and properties of Bacillus subtilis nucleoside diphosphokinase
    • Sedmak J & Ramaley R (1971) Purification and properties of Bacillus subtilis nucleoside diphosphokinase. J Biol Chem 246: 5365-5372.
    • (1971) J Biol Chem , vol.246 , pp. 5365-5372
    • Sedmak, J.1    Ramaley, R.2
  • 18
    • 0842303216 scopus 로고    scopus 로고
    • Highly efficient renaturation of beta-lactamase isolated from moderately halophilic bacteria
    • Tokunaga H, Ishibashi M, Arakawa T & Tokunaga M (2004) Highly efficient renaturation of beta-lactamase isolated from moderately halophilic bacteria. FEBS Lett 558: 7-12.
    • (2004) FEBS Lett , vol.558 , pp. 7-12
    • Tokunaga, H.1    Ishibashi, M.2    Arakawa, T.3    Tokunaga, M.4
  • 19
    • 33646394637 scopus 로고    scopus 로고
    • Contribution of halophilic nucleoside diphosphate kinase sequence to the heat stability of chimeric molecule
    • Tokunaga H, Oda Y, Yonezawa Y, Arakawa T & Tokunaga M (2006) Contribution of halophilic nucleoside diphosphate kinase sequence to the heat stability of chimeric molecule. Protein Pept Lett 13: 525-530.
    • (2006) Protein Pept Lett , vol.13 , pp. 525-530
    • Tokunaga, H.1    Oda, Y.2    Yonezawa, Y.3    Arakawa, T.4    Tokunaga, M.5
  • 20
    • 0031810562 scopus 로고    scopus 로고
    • Biology of moderately halophilic aerobic bacteria
    • Ventosa A, Nietro JJ & Oren A (1998) Biology of moderately halophilic aerobic bacteria. Microbiol Mol Biol Rev 62: 504-544.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 504-544
    • Ventosa, A.1    Nietro, J.J.2    Oren, A.3
  • 21
    • 0035490496 scopus 로고    scopus 로고
    • Characterization of nucleoside diphosphate kinase from moderately halophilic eubacteria
    • Yonezawa Y, Tokunaga H, Ishibashi M & Tokunaga M (2001) Characterization of nucleoside diphosphate kinase from moderately halophilic eubacteria. Biosci Biotechnol Biochem 65: 2343-2346.
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 2343-2346
    • Yonezawa, Y.1    Tokunaga, H.2    Ishibashi, M.3    Tokunaga, M.4
  • 22
    • 0042284085 scopus 로고    scopus 로고
    • Cloning, expression, and efficient purification in Escherichia coli of a halophilic nucleoside diphosphate kinase from the moderate halophile Halomonas sp. #593
    • Yonezawa Y, Tokunaga H, Ishibashi M, Taura S & Tokunaga M (2003) Cloning, expression, and efficient purification in Escherichia coli of a halophilic nucleoside diphosphate kinase from the moderate halophile Halomonas sp. #593. Protein Expr Purif 27: 128-133.
    • (2003) Protein Expr Purif , vol.27 , pp. 128-133
    • Yonezawa, Y.1    Tokunaga, H.2    Ishibashi, M.3    Taura, S.4    Tokunaga, M.5


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